The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Sirt3-Mediated Deacetylation of Evolutionarily Conserved Lysine 122 Regulates MnSOD Activity in Response to Stress
Open accessAbstract
Genetic deletion of the mitochondrial deacetylase sirtuin-3 (Sirt3) results in increased mitochondrial superoxide, a tumor-permissive environment, and mammary tumor development. MnSOD contains a nutrient- and ionizing radiation (IR)-dependent reversible acetyl-lysine that is hyperacetylated in Sirt3⁻/⁻ livers at 3 months of age. Livers of Sirt3⁻/⁻ mice exhibit decreased MnSOD activity, but not immunoreactive protein, relative to wild-type livers. Reintroduction of wild-type but not deacetylation null Sirt3 into Sirt3⁻/⁻ MEFs deacetylated lysine and restored MnSOD activity. Site-directed mutagenesis of MnSOD lysine 122 to an arginine, mimicking deacetylation (lenti-MnSOD(K122-R)), increased MnSOD activity when expressed in MnSOD⁻/⁻ MEFs, suggesting acetylation directly regulates function. Furthermore, infection of Sirt3⁻/⁻ MEFs with lenti-MnSOD(K122-R) inhibited in vitro immortalization by an oncogene (Ras), inhibited IR-induced genomic instability, and decreased mitochondrial superoxide. Finally, IR was unable to induce MnSOD deacetylation or activity in Sirt3⁻/⁻ livers, and these irradiated livers displayed significant IR-induced cell damage and microvacuolization in their hepatocytes.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“SIRT3 may also directly control the rate of ROS production by deacetylating manganese superoxide dismutase, a major mitochondrial antioxidant enzyme”
From The Hallmarks of Aging (2013) · cites this paper as Tao et al., 2010
Experimental — accuracy not yet measuredIn the citing paper
“MnSOD also carries glutarylation, succinylation, and acetylation at functionally required lysine residues near its active site, K122 in particular bears all three modifications ((Tao et al. 2010)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tao et al. 2010
In the citing paper
“The mitochondrial SIRT3 deacetylates two of these enzymes: manganese superoxide dismutase (MnSOD) (Tao et al. 2010) and isocitrate dehydrogenase 2 (IDH2)(Someya et al. 2010).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Tao et al. 2010
In the citing paper
“Recently, two enzymes that have a role in the detoxification of ROS were demonstrated to be direct targets of SirT3 (Qiu et al., 2010; Someya et al., 2010; Tao et al., 2010).”
From SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production (2011) · cites this paper as Tao et al., 2010
In the citing paper
“More importantly, SIRT3 can directly bind and deacetylate SOD2, leading to increased SOD2 activity and subsequently exerting significant effects on mtROS homeostasis and NLRP3 inflammasome activation.18, 19, 20”
From Trimethylamine‐N‐Oxide Induces Vascular Inflammation by Activating the NLRP3 Inflammasome Through the SIRT3‐SOD2‐mtROS Signaling Pathway (2017) · cites this paper as [20]
In the citing paper
“SOD2 activity is known to be tightly regulated via acetylation at its lysine residues.20”
From Trimethylamine‐N‐Oxide Induces Vascular Inflammation by Activating the NLRP3 Inflammasome Through the SIRT3‐SOD2‐mtROS Signaling Pathway (2017) · cites this paper as [20]
In the citing paper
“because SOD2 is mainly regulated by the deacetylation of specific conserved lysines in a reaction catalyzed by the mitochondrial sirtuin SIRT3,20”
From Trimethylamine‐N‐Oxide Induces Vascular Inflammation by Activating the NLRP3 Inflammasome Through the SIRT3‐SOD2‐mtROS Signaling Pathway (2017) · cites this paper as [20]
In the citing paper
“SIRT3 deacetylates a number of mitochondrial proteins including SOD2, which is responsible for limiting the accumulation of mtROS.20”
From Trimethylamine‐N‐Oxide Induces Vascular Inflammation by Activating the NLRP3 Inflammasome Through the SIRT3‐SOD2‐mtROS Signaling Pathway (2017) · cites this paper as [20]
In the citing paper
“MnSOD activity and stability are highly regulated by post-translational modifications, including protein acetylation in the mitochondria (Takahashi et al., 2011; Tao et al., 2010).”
From mTOR inhibition prevents epithelial stem cell senescence and protects from radiation-induced mucositis (2012) · cites this paper as Tao et al., 2010
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The RB and p53 pathways in cancer
Sherr, C. J., & McCormick, F. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00102-2 · Cited by 1,690
Recent progress in the biology and physiology of sirtuins
Finkel, T., Deng, C., & Mostoslavsky, R. (2009) · Nature · doi:10.1038/nature08197 · Cited by 1,506
A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
Ahn, B.-H., Kim, H.-S., Song, S., Lee, I. H., Liu, J., Vassilopoulos, A., Deng, C.-X., & Finkel, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803790105 · Cited by 1,291
Self-citationMammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation
Lombard, D. B., Alt, F. W., Cheng, H.-L., Bunkenborg, J., Streeper, R. S., Mostoslavsky, R., Kim, J., Yancopoulos, G., Valenzuela, D., Murphy, A., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01636-07 · Cited by 1,216
Revollo, J. R., Grimm, A. A., & Imai, S.-I. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408388200 · Cited by 1,010
Kim, H.-S., Patel, K., Muldoon-Jacobs, K., Bisht, K. S., Aykin-Burns, N., Pennington, J. D., van der Meer, R., Nguyen, P., Savage, J., Owens, K. M., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.11.023 · Cited by 785
Self-citationAn assay for superoxide dismutase activity in mammalian tissue homogenates
Spitz, D. R., & Oberley, L. W. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90192-9 · Cited by 751
Self-citationSchwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., & Verdin, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603968103 · Cited by 705
SIRT1 Deacetylates and Positively Regulates the Nuclear Receptor LXR
Li, X., Zhang, S., Blander, G., Tse, J. G., Krieger, M., & Guarente, L. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.032 · Cited by 649
Schwer, B., North, B. J., Frye, R. A., Ott, M., & Verdin, E. M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200205057 · Cited by 599
Flagged first, then by citations
Cited by
Sorted by citations
Items 501–600 of 901
Zhang, L., Ren, X., Cheng, Y., Huber-Keener, K. J., Liu, X., Zhang, Y., Yuan, Y., Yang, J. W., Liu, C., & Yang, J. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.06.032 · Cited by 33
Winnik, S. H., Gaul, D. S., Siciliani, G., Lohmann, C., Pasterk, L., Calatayud, N., Weber, J., Eriksson, U., Auwerx, J. H., van Tits, L. J., et al. (2016) · Basic Research in Cardiology · doi:10.1007/s00395-016-0552-7 · Cited by 33
SIRT3/6: an amazing challenge and opportunity in the fight against fibrosis and aging
Wei, W., Li, T. X., Chen, J., Fan, Z., Gao, F., Yu, Z., & Jiang, Y. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05093-z · Cited by 34
SIRT3 mediates decrease of oxidative damage and prevention of ageing in porcine fetal fibroblasts
Xie, X., Wang, L., Zhao, B., Chen, Y., & Li, J. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.01.010 · Cited by 33
Barjaktarović, Ž., Merl‐Pham, J., Braga-Tanaka, I., Tanaka, S., Hauck, S. M., Saran, A., Mancuso, M., Atkinson, M. J., Tapio, S., & Azimzadeh, O. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20205239 · Cited by 32
Guo, R. Z., Liu, N., Liu, H., Zhang, J., Zhang, H., Wang, Y., Baruscotti, M., Zhao, L., & Wáng, Y. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153171 · Cited by 32
Neprilysin Inhibition in the Prevention of Anthracycline-Induced Cardiotoxicity
Sobiborowicz, A., Kamińska, K., & Cudnoch‐Jędrzejewska, A. (2023) · Cancers · doi:10.3390/cancers15010312 · Cited by 35
The Protein Deacetylase SIRT3 Prevents Oxidative Stress-induced Keratinocyte Differentiation
Bause, A. S., Matsui, M. S., & Haigis, M. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.472324 · Cited by 34
Molecular mechanisms underlying methotrexate-induced intestinal injury and protective strategies
Ali, G. F., Hassanein, E. H. M., & Mohamed, W. R. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03164-x · Cited by 31
Mitochondrial sirtuins, key regulators of aging
Ji, Z., Liu, G., & Qu, J. T. (2025) · Life Medicine · doi:10.1093/lifemedi/lnaf019 · Cited by 32
Yoon, S. P., & Kim, J. (2016) · Anatomy & Cell Biology · doi:10.5115/acb.2016.49.3.165 · Cited by 31
Yang, K.-E., Jang, H.-J., Hwang, I., Hong, E. M., Lee, M. G., Lee, S., Jang, I., & Choi, J.-S. (2019) · Journal of Ginseng Research · doi:10.1016/j.jgr.2019.08.002 · Cited by 31
Avilkina, V., Chauveau, C., & Mhenni, O. G. (2021) · Bone · doi:10.1016/j.bone.2021.116232 · Cited by 33
Sirtuins in Hematological Aging and Malignancy
Roth, M., Wang, Z., & Chen, W. (2013) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.2013010187 · Cited by 31
Tian, Y., Wen, Z., Lei, L., Li, F., Zhao, J., Zhi, Q., Li, F., Yin, R., & Ming, J. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103464 · Cited by 30
Yun, U. J., & Yang, D. K. (2020) · Antioxidants · doi:10.3390/antiox9111163 · Cited by 30
Expanding the link between circadian rhythms and redox metabolism of epigenetic control
Sato, T., & Greco, C. M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.009 · Cited by 30
Rohrbach, S., Aslam, M., Niemann, B., & Schulz, R. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12650 · Cited by 31
Resveratrol Stimulates Cortisol Biosynthesis by Activating SIRT-Dependent Deacetylation of P450scc
Li, D., Dammer, E. B., & Sewer, M. B. (2012) · Endocrinology · doi:10.1210/en.2011-2088 · Cited by 30
Sirtuin 3 Deficiency Does Not Augment Hypoxia-Induced Pulmonary Hypertension
Waypa, G. B., Osborne, S. W., Marks, J. D., Berkelhamer, S. K., Kondapalli, J., & Schumacker, P. T. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0191oc · Cited by 32
Kenny, T. C., & Germain, D. (2017) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-017-9722-z · Cited by 31
Rezaei, M., Keshtzar, E., Khodayar, M. J., & Javadipour, M. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.10.025 · Cited by 31
Li, A., Yi, J., Li, X., & Zhou, J. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.595800 · Cited by 27
Anakinra Activates Superoxide Dismutase 2 to Mitigate Inflammasome Activity
Pariano, M., Pieroni, S., LUCA, A. D., Iannitti, R. G., Borghi, M., Puccetti, M., Giovagnoli, S., Renga, G., D’Onofrio, F., Bellet, M. M., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126531 · Cited by 29
Hao, K., Wang, H., Zhang, Y., Xie, X., Huang, H., Cheng Ann, C. H. E. N., Xu, S., Xu, R., Shu, C., Liu, Z., et al. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02591-y · Cited by 26
Zhang, L., Chen, C., Kang, P. T., Jin, Z., & Chen, Y. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.022 · Cited by 32
Kichukova, T. M., Popov, N. T., Ivanov, H. Y., & Vachev, T. I. (2016) · Folia Medica · doi:10.1515/folmed-2015-0035 · Cited by 28
Mechanisms of transcription factor acetylation and consequences in hearts
Thiagarajan, D., Vedantham, S., Ananthakrishnan, R., Schmidt, A. M., & Ramasamy, R. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.011 · Cited by 29
Jiang, T., Liu, Y., Meng, Q., Lv, X., Yue, Z., Ding, W., Liu, T., & Cui, X. (2019) · Surgery · doi:10.1016/j.surg.2018.12.018 · Cited by 28
Zhou, S., Sun, L., Qian, S., Ma, Y., Ma, R., Dong, Y., Shi, Y., Jiang, S., Ye, H., Shen, Z., et al. (2021) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-020-00244-7 · Cited by 28
Zhao, Q., Zhou, J., Li, F., Guo, S., Zhang, L. N., Li, J., Qi, Q., & Shi, Y. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.910963 · Cited by 28
Xu, J., Kitada, M., & Koya, D. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165756 · Cited by 30
Ye, H., Yi, L., Yang, J., Wu, Y., Dong, L.-Y., Zhong, Y., Luo, Y., & Wang, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-58375-2 · Cited by 28
Mitochondrial targeted antioxidants as potential therapy for huntington’s disease
Upadhayay, S., & Kumar, P. (2024) · Pharmacological Reports · doi:10.1007/s43440-024-00619-z · Cited by 30
Tian, Y., & Zhang, J. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.8469 · Cited by 27
Bover, A. G., Hernández‐López, R., Alorda-Clara, M., de la Rosa, J. M. I., Falcó, E., Fernández, T., Torrens‐Mas, M., Roca, P., Oliver, J., Sastre‐Serra, J., et al. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105698 · Cited by 26
Yao, Y. Y., Ling, E., & Lü, D. (2020) · PubMed · doi:10.14670/hh-18-239 · Cited by 26
Bai, Y., Yang, Y., Gao, Y., Lin, D., Wang, Z., & Ma, J. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174157 · Cited by 28
Nebivolol stimulates mitochondrial biogenesis in 3T3-L1 adipocytes
Huang, C., Chen, D., Xie, Q., Yang, Y., & Shen, W. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.07.055 · Cited by 26
Selvam, M. K. P., Samanta, L., & Agarwal, A. K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093155 · Cited by 27
Zhu, X., Ma, E., Ge, Y., Meng, Y., Guo, X., Peng, J., Zhu, W., Ren, D., & Wo, D. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116476 · Cited by 26
Shulyakova, N., Sidorova‐Darmos, E., Fong, J., Zhang, G., Mills, L. R., & Eubanks, J. H. (2014) · Brain Research · doi:10.1016/j.brainres.2014.08.066 · Cited by 26
Mitochondrial Acetylation and Genetic Models of Parkinson's Disease
Auburger, G. W. J., Gispert, S., & Jendrach, M. (2014) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394625-6.00006-4 · Cited by 27
You, J., Yue, Z., Chen, S., Chen, Y., Lu, X., Zhang, X., Shen, P., Li, J., Han, Q., Li, Z., et al. (2016) · Acta Physiologica · doi:10.1111/apha.12800 · Cited by 26
Sirtuins in female meiosis and in reproductive longevity
Vázquez, B. N., Vaquero, A., & Schindler, K. (2020) · Molecular Reproduction and Development · doi:10.1002/mrd.23437 · Cited by 26
Masgras, I., Cannino, G., Ciscato, F., Sànchez‐Martìn, C., Darvishi, F. B., Scantamburlo, F., Pizzi, M., Menga, A., Fregona, D., Castegna, A., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00991-4 · Cited by 26
The roles of sirtuins in ferroptosis
Zeng, J., Guo, J., Huang, S., Cheng, Y., Luo, F., Xu, X., Chen, R., Ma, G., & Wang, Y. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1131201 · Cited by 29
Roles of SIRT3 in aging and aging-related diseases
You, Y., & Wang, Z. (2025) · International Journal of Biological Sciences · doi:10.7150/ijbs.115518 · Cited by 26
Wang, S., Yang, J., Lin, T., Huang, S., Ma, J., & Xu, X. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11094 · Cited by 25
Chen, H., Zhang, D., Zhang, Z., Li, M., & Wu, H.-F. (2021) · Genes & Genomics · doi:10.1007/s13258-021-01145-5 · Cited by 25
Ubaida‐Mohien, C., Spendiff, S., Lyashkov, A. E., Moaddel, R., MacMillan, N. J., Filion, M., Morais, J. A., Taivassalo, T., Ferrucci, L., & Hepple, R. T. (2022) · eLife · doi:10.7554/elife.74335 · Cited by 25
Hu, X., & Zhang, L. (2022) · Antioxidants · doi:10.3390/antiox11122432 · Cited by 22
Zwergel, C., Aventaggiato, M., Garbo, S., Bello, E. D., Fassari, B., Noce, B., Castiello, C., Lambona, C., Barreca, F., Rotili, D., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00337 · Cited by 25
Genetic and Functional Sequence Variants of the SIRT3 Gene Promoter in Myocardial Infarction
Yin, X., Pang, S., Huang, J. A., Cui, Y., & Yan, B. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153815 · Cited by 25
Wang, Y., Chen, J., Kong, W.-Z., Zhu, R., Liang, K., Kan, Q., Lou, Y., & Liu, X. (2017) · Archives of Medical Research · doi:10.1016/j.arcmed.2017.11.016 · Cited by 25
Xie, Z., Cao, B., Wang, T., Lei, Q., Kang, T., Ge, C.-Y., Gao, W., & Hui, H. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.07.017 · Cited by 25
Sirtuin-3 modulates Bak- and Bax-dependent apoptosis
Verma, M., Shulga, N., & Pastorino, J. G. (2012) · Journal of Cell Science · doi:10.1242/jcs.115188 · Cited by 24
RetractedYu, J. D., & Miyamoto, S. (2021) · Cells · doi:10.3390/cells10123330 · Cited by 25
Chen, D., Shao, H.-Y., Yang, L., & Hu, J. (2022) · Natural Products and Bioprospecting · doi:10.1007/s13659-022-00323-6 · Cited by 24
Nicotinamide Mononucleotide Administration Amends Protein Acetylome of Aged Mouse Liver
Luo, C., Ding, W., Zhu, S., Chen, Y., Liu, X., & Deng, H. (2022) · Cells · doi:10.3390/cells11101654 · Cited by 26
The relationship between atrial fibrillation and NLRP3 inflammasome: a gut microbiota perspective
Xing, Y., Yan, L., Li, X., Xu, Z., Wu, X., Gao, H., Chen, Y., Ma, X., Liu, J., & Zhang, J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1273524 · Cited by 29
Intersections between mitochondrial sirtuin signaling and tumor cell metabolism
Herrera, K. N. G., Lee, J. J., & Haigis, M. C. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1031879 · Cited by 25
Wirth, M., Karaca, S., Wenzel, D., Ho, L., Tishkoff, D. X., Lombard, D. B., Verdin, E. M., Urlaub, H., Jedrusik, M. A., & Fischle, W. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.02.002 · Cited by 22
Neuroprotective role of retinal SIRT3 against acute photo-stress
Ban, N., Ozawa, Y., Osada, H., Lin, J. B., Toda, E., 渡辺, 光., Yuki, K., Kubota, S., Apte, R. S., & Tsubota, K. (2017) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-017-0017-8 · Cited by 24
Du, Z.-J., Zhang, W., Wang, S., Zhang, J., He, J., Wang, Y., Dong, Y., & Huo, M. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28326 · Cited by 25
Sirt3 is dispensable for oocyte quality and female fertility in lean and obese mice
Iljas, J. D., & Homer, H. A. (2020) · The FASEB Journal · doi:10.1096/fj.202000153r · Cited by 24
Mitochondria-targeted inhibitors of the human SIRT3 lysine deacetylase
Troelsen, K. R., Bæk, M., Nielsen, A. L., Madsen, A. S., Rajabi, N., & Olsen, C. A. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00216j · Cited by 24
Dikalova, A., Ao, M., Tkachuk, L., & Dikalov, S. (2024) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00162.2024 · Cited by 23
Kobayashi, M., Takeda, K., Narita, T., Nagai, K., Okita, N., Sudo, Y., Miura, Y., Tsumoto, H., Nakagawa, Y., Shimano, H., et al. (2017) · FEBS Letters · doi:10.1002/1873-3468.12914 · Cited by 23
Ma, L., Shi, H., Li, Y., Gao, W., Guo, J., Zhu, J., Dong, Z., Sun, A., Zou, Y., & Ge, J. (2021) · 中国科学通报：英文版 · doi:10.1016/j.scib.2021.04.008 · Cited by 23
Zhang, X., Zhang, Y., Sun, A., & Ge, J. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.04.001 · Cited by 24
Barbosa, P. O., de Souza, M. O., Silva, M. P. S., Santos, G. T., Silva, M. E., Bermano, G., & de Freitas, R. N. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111627 · Cited by 23
Nguyen, T., Caito, S. W., Zackert, W. E., West, J. D., Shijun, Z., Aschner, M., Fessel, J. P., & Roberts, L. J. (2016) · Aging · doi:10.18632/aging.101011 · Cited by 23
Galvani, F., Cammarota, M., Vacondio, F., Rivara, S., & Boscia, F. (2024) · Journal of Pineal Research · doi:10.1111/jpi.70008 · Cited by 24
Joardar, N., Guevara‐Flores, A., Martínez-González, J. D. J., & Babu, S. P. S. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.09.096 · Cited by 22
Li, Y., Jia, X. T., Tang, N., Huiyuan, T., Xia, R. M., & Cheng, Y. (2021) · Food & Function · doi:10.1039/d1fo00978h · Cited by 24
The structure–function relationships and physiological roles of MnSOD mutants
Bonetta, R. (2022) · Bioscience Reports · doi:10.1042/bsr20220202 · Cited by 24
Impact of acetylation on tumor metabolism
Zhao, D., Li, F.-L., Cheng, Z., & Lei, Q. (2014) · Molecular & Cellular Oncology · doi:10.4161/23723548.2014.963452 · Cited by 24
Acetylation control of metabolic enzymes in cancer: an updated version
Huang, W., Wang, Z., & Lei, Q. (2014) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt154 · Cited by 23
Alterations of sirtuins in mitochondrial cytochrome c-oxidase deficiency
Potthast, A. B., Heuer, T., Warneke, S. J., & Das, A. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186517 · Cited by 22
Mi, C., Qin, X., Hou, Z., & Gao, F. (2019) · Brazilian Journal of Medical and Biological Research · doi:10.1590/1414-431x20198009 · Cited by 22
Yang, N., Ma, H., Jiang, Z., Niu, L., Zhang, X., Liu, Y., Wang, Y., Cheng, S., Deng, Y., Qi, H., et al. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.07.029 · Cited by 22
Lam, Y. T. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7095901 · Cited by 22
Translational Regulation of GPx-1 and GPx-4 by the mTOR Pathway
Reinke, E. N., Ekoue, D. N., Bera, S., Mahmud, N., & Diamond, A. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093472 · Cited by 22
Gao, Y., Zhu, Y., Tran, E. L., Tokars, V. L., Dean, A. E., Quan, S., & Gius, D. R. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.51184 · Cited by 22
Self-citationCao, X., Wu, Y., Hong, H., & Tian, X. Y. (2022) · Antioxidants · doi:10.3390/antiox11040706 · Cited by 21
Gong, H., Liu, J., Xue, Z., Wang, W., Li, C., Xu, F., Du, Y. L., & Lyu, X. (2022) · Journal of Clinical Laboratory Analysis · doi:10.1002/jcla.24586 · Cited by 21
SIRT3: Striking at the heart of aging
Liu, Y., Zhang, D., & Chen, D. (2011) · Aging · doi:10.18632/aging.100256 · Cited by 21
Sirtuin (Sirt) 3 Overexpression Prevents Retinopathy in Streptozotocin-Induced Diabetic Rats
Mao, X., Cheng, Y., Peng, K.-S., & You, Z. (2020) · Medical Science Monitor · doi:10.12659/msm.920883 · Cited by 21
Hitchler, M. J., & Domann, F. E. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.008 · Cited by 20
Multifaced role of protein deacetylase sirtuins in neurodegenerative disease
Gupta, R. V., Ambasta, R. K., & Kumar, P. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.10.047 · Cited by 20
Liang, H., Lu, P.-X., Chu, L.-L., Li, G., Li, C., Chen, X., Zhang, J., Song, J., Zhang, T., Luo, Y., et al. (2023) · Phytochemistry · doi:10.1016/j.phytochem.2023.113744 · Cited by 20
Combination of ACE inhibitor with nicorandil provides further protection in chronic kidney disease
Shiraishi, T., Tamura, Y., Taniguchi, K., Higaki, M., Ueda, S., Shima, T., Nagura, M., Nakagawa, T., Johnson, R. J., & Uchida, S. (2014) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00521.2014 · Cited by 20
Gudiksen, A., Qoqaj, A., Ringholm, S., Wojtaszewski, J. F. P., Plomgaard, P., & Pilegaard, H. (2021) · The Journals of Gerontology Series A · doi:10.1093/gerona/glab356 · Cited by 21
Key Molecular Mechanisms of Aging, Biomarkers, and Potential Interventions
Proshkina, E., Solovev, I. A., Shaposhnikov, M. V., & Moskalev, A. (2020) · Molecular Biology · doi:10.1134/s0026893320060096 · Cited by 21
Tan, X., Zhou, Y., Agarwal, A., Lim, M., Xu, Y., Zhu, Y., O'Brien, J., Tran, E. L., Zheng, J., Gius, D. R., et al. (2020) · PubMed Central · Cited by 18
Self-citationOpazo, J. C., Vandewege, M. W., Hoffmann, F. G., Zavala, K., Meléndez, C., Luchsinger, C., Cavieres, V. A., Vargas‐Chacoff, L., Morera, F. J., Burgos, P. V., et al. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad014 · Cited by 19
Martell, E., Kuzmychova, H., Kaul, E., Senthil, H., Chowdhury, S. R., Morrison, L. C., Fresnoza, A. L., Zagozewski, J. L., Venugopal, C., Anderson, C. M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38049-9 · Cited by 20
Dong, Y., Li, T., Wang, S.-S., Hu, Y.-H., Liu, Y., Zhang, F., Sun, T.-S., Zhang, C.-J., Du, Q., & Li, W. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118237 · Cited by 19
Saha, B., Pallatt, S., Banerjee, A., Banerjee, A. G., Pathak, R., & Pathak, S. (2024) · Cells · doi:10.3390/cells13181560 · Cited by 20
Metadata
- Authors
- Tao, R., Coleman, M. C., Pennington, J. D., Ozden, O., Park, S.-H., Jiang, H., Kim, H.-S., Flynn, C. R., Hill, S., Hayes McDonald, W., Olivier, A. K., Spitz, D. R., & Gius, D.
- Affiliations
- National Institutes of Health (US)
- University of Iowa (US)
- Vanderbilt University Medical Center (US)
- Vanderbilt University (US)
- Corresponding author
- Gius, David
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 40
- Issue
- 6
- Pages
- 893-904
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3266626
- OpenAlex
- W2039374791
- Cited by
- 899
- References
- 24
- Citations by year
- 2026: 28 · 2025: 35 · 2024: 36 · 2023: 44 · 2022: 48 · 2021: 72 · 2020: 64 · 2019: 66 · 2018: 62 · 2017: 80 · 2016: 71 · 2015: 61 · 2014: 64 · 2013: 68 · 2012: 58
- FWCI
- 21.31
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 959 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (F30AG030839)
- National Cancer Institute (P50 CA98131, R01CA133114, R01CA152601, P50CA098131, T32CA078586, P30CA086862)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- SIRT3, manganese superoxide dismutase, protein acetylation, deacetylation, mitochondrial superoxide, ionizing radiation, radiation-induced genomic instability, oncogenic Ras, mammary tumors, liver, hepatocyte injury, mitochondrial deacetylase, tumor microenvironment
- MeSH terms
- Acetylation, Animals, Arginine, Cell Line, Lysine, Superoxide Dismutase, Mutagenesis, Site-Directed, Conserved Sequence, Oxidative Stress, Evolution, Molecular, Mice, Sirtuin 3
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
